2RLW

Three-Dimensional Structure of the two Peptides that Constitute the Two-Peptide Bacteriocin Plantaracin EF

2RLW の概要

• エントリーDOI: 10.2210/pdb2rlw/pdb
• 関連するPDBエントリー: 2JUI
• 分子名称: PlnF (1 entity in total)
• 機能のキーワード: peptide plnf, toxin
• 由来する生物種: Lactobacillus plantarum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3709.18

構造登録者

Fimland, N.,Rogne, P.,Fimland, G.,Nissen-Meyer, J.,Kristiansen, P. (登録日: 2007-08-27, 公開日: 2008-07-01, 最終更新日: 2024-05-22)

主引用文献

Fimland, N.,Rogne, P.,Fimland, G.,Nissen-Meyer, J.,Kristiansen, P.E.
Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF
Biochim.Biophys.Acta, 1784:1711-1719, 2008

PubMed Abstract: The three-dimensional structures of the two peptides plantaricin E (plnE; 33 residues) and plantaricin F (plnF; 34 residues) constituting the two-peptide bacteriocin plantaricin EF (plnEF) have been determined by nuclear magnetic resonance (NMR) spectroscopy in the presence of DPC micelles. PlnE has an N-terminal alpha-helix (residues 10-21), and a C-terminal alpha-helix-like structure (residues 25-31). PlnF has a long central alpha-helix (residues 7-32) with a kink of 38+/-7 degrees at Pro20. There is some flexibility in the helix in the kink region. Both helices in plnE are amphiphilic, while the helix in plnF is polar in its N-terminal half and amphiphilic in its C-terminal half. The alpha-helical content obtained by NMR spectroscopy is in agreement with CD studies. PlnE has two GxxxG motifs which are putative helix-helix interaction motifs, one at residues 5 to 9 and one at residues 20 to 24, while plnF has one such motif at residues 30 to 34. The peptides are flexible in these GxxxG regions. It is suggested that the two peptides lie parallel in a staggered fashion relative to each other and interact through helix-helix interactions involving the GxxxG motifs.

PubMed: 18555030
DOI: 10.1016/j.bbapap.2008.05.003

実験手法

SOLUTION NMR